[Fluorescence study on the interaction of salicylic acid and bovine serum albumin].

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Xiao HR, Sheng LQ, Shi CH, Xu XL, Xie YS, Liu QL

[Fluorescence study on the interaction of salicylic acid and bovine serum albumin].

Guang Pu Xue Yu Guang Pu Fen Xi. 2004 Jan;24(1):78-81.

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15768982 [ View in PubMed

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Abstract

The interaction between salicylic acid and bovine serum albumin has been studied by fluorescence spectroscopy. The results show that the quenching mechanism of the combination of bovine serum albumin with salicylic acid is a static quenching procedure, the quenching constant K(sv) is 1.097 x 10(4) (mol x L(-1))(-1), and the equilibrium constant is 7.377 x 10(4). The number of binding sites is 1 and it is a strong one. When the ratio of molar concentration of salicylic acid to bovine serum albumin is lower than 1:1, it binds to Trp residue first but it doesn't result in any microenvironment changes of Trp residue. The binding distance between salicylic acid and bovine serum albumin and the energy transfer efficiency were obtained based on the theory of Forester spectroscopy energy transfer.

DrugBank Data that Cites this Article

Drug Carriers

Drug	Carrier	Kind	Organism	Pharmacological Action	Actions
Salicylic acid	Serum albumin	Protein	Humans	No	Other/unknown	Details